The purification and stabilization of human interferon has become increasingly important as its use as an antiviral and anticancer agent grows. The most powerful technique for purifying interferon from media of interferon-producing cells involves binding of the protein to a hydrophobic ligand carrying primary amino groups, such as Cibarcron Blue F3G-A, and its subsequent elution by solutions containing ethylene glycol (Jankowski, et al., 1976, Biochemistry 15:5182-5187; Knight and Fahey, 1981, J. Biol. Chem. 256:3609-3611). A slight modification of the procedure starting from "serum-free" media was patented by Knight U.S. patent application No. 84,632, filed Oct. 12, 1979) but in our hands the advantage in purity is more than offset by yields which are diminished 4-10 fold and, more importantly, by the need to use ethylene glycol.